ID H0ZK86_TAEGU Unreviewed; 1185 AA.
AC H0ZK86;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cohesin subunit SA {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=SCC3 homolog {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=Stromal antigen {ECO:0000256|RuleBase:RU369063};
GN Name=LOC100221786 {ECO:0000313|Ensembl:ENSTGUP00000011006.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000011006.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000011006.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000011006.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBUNIT: Part of the cohesin complex which is composed of a heterodimer
CC between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached
CC via their hinge domain, and RAD21 which link them at their heads, and
CC one STAG protein. {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369063}.
CC Chromosome {ECO:0000256|RuleBase:RU369063}. Chromosome, centromere
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000256|ARBA:ARBA00005486,
CC ECO:0000256|RuleBase:RU369063}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H0ZK86; -.
DR STRING; 59729.ENSTGUP00000011006; -.
DR Ensembl; ENSTGUT00000011121.2; ENSTGUP00000011006.2; ENSTGUG00000010652.2.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR InParanoid; H0ZK86; -.
DR OMA; YILCREE; -.
DR TreeFam; TF314604; -.
DR Proteomes; UP000007754; Chromosome 1.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-UniRule.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:UniProtKB-UniRule.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF2; SCD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR Pfam; PF21581; SCD; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51425; SCD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU369063};
KW Cell division {ECO:0000256|RuleBase:RU369063};
KW Chromosome {ECO:0000256|RuleBase:RU369063};
KW Chromosome partition {ECO:0000256|RuleBase:RU369063};
KW Nucleus {ECO:0000256|RuleBase:RU369063};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT DOMAIN 307..392
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1073..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 136121 MW; AC82A9A263A5EBC3 CRC64;
MYGSRSPRRE NAVHDETVLE SAAQNGTYVR NGNLKTPREK QKVREQCENI RRSSTAARRA
SQLQNGEVVE AVTLFEVVSM GKQAMQSVVV DWVEAYKQDR NVALLDLINF FIQCSGCQGM
VTAEMFQSLY KKDVMQKMTE TFDKETGLQY KKFVAYPWIL TVTWPVDMDN EDYPLIRTGP
YWKKFKANFC EFIAVLVQQC QCSILYDNYL MDTIISLLTG LADSMVRAFR HTSTLAAMKL
LTAVVSIHLN LDVSKHNAQR LYEVEKKRLS GRRTSYRLDQ LERKRKEYEH KLLEIQNMMN
AIFKGTFLNR YRDVIPEIRA TCIEEIGSWI KMSPDAFLND SYLKYVGWML YDKQAEVRLK
CLLGLQGIYS RKELVSRMDL FTNRFKDRIV SMPLDKDHEV AVQAMKLLML MSQNCEDVLS
AEDCEMLYQF VYTTHRPLAV AAGEFLYKRL LSHEGDKKVQ PEGGGKFGAS TDQLKRLIHF
FLKGELHKHV TYLVDSLWDW AGKFLKDWEC MTSLLLKNAE EVGEALSDAQ ESVLIEIILA
TVREAAEGHP PVGRGAAKKI LSVKEKKIQL EDCKKITEHF IMVLPQLLAK YSTDAQKVAN
LLQIPQYYDL DVYSTRHLEK HLDALLREIK DIVAKHSDMS VLEASSRTYY ILCREEIAIY
SQVDCARTQM IDELVKQLNQ LLDCFWKKEG GFCTDAGEIS RMHSTLRRVA AFHNAHDLTK
WNLYDKTLRF LVFETEHGRL PVLIILPALQ CTYFSLLWQL AAVSEHSPKE TLFPLRKQLR
HFSQICTCFL HHKEKDVREK AFMILCDWLL ILSHLYSNNE EAVGLLGYLP STQLQEKLFS
FIQEHVFMDG EEEKKDLTEE GKDETCKLDD LHKKRSLLAA YCKLIVYNVV EMTAAAEIYK
YYVKTYSDFG DIIKETLSKT RCNNKIQSAK TLILCLQQLF QTHAESQDSS NGVDFSSPSF
ANIKELARRF ALTFGWDQVK SRESIAMIHK EGIEFAFQGT TGIDGKCFPP NLSFLVIISE
FSNKLLKPDK RLVYSYLQRY ITEPLSCRGD KWQPLVWYRN SLLANEDEES SVLGSLGERH
PVGSSKTSSF KRKLSNGSLP ETSQTEAGSK APEQQCASQL PSAAGKSRKR LKSKEMRLQE
HLPFLCPGGL HRRYCKDEVK TEDVSEEGPE DTVEDVDVIG TDQDS
//
